Biology:GHKL domain
| Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
 Structure of the N-terminal domain of the yeast Hsp90 chaperone.[1] | |||||||||||
| Identifiers | |||||||||||
| Symbol | HATPase_c | ||||||||||
| Pfam | PF02518 | ||||||||||
| InterPro | IPR003594 | ||||||||||
| SMART | HATPase_c | ||||||||||
| SCOP2 | 1ei1 / SCOPe / SUPFAM | ||||||||||
| CDD | cd00075 | ||||||||||
| |||||||||||
The GHKL domain (Gyrase, Hsp90, Histidine Kinase, MutL) is an evolutionary conserved protein domain.[2] It is an ATPase domain found in several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases,[3] heat shock protein HSP90,[4][5][6] phytochrome-like ATPases and DNA mismatch repair proteins.
More information about this protein can be found at Protein of the Month: DNA Topoisomerase.[7]
Structure
The fold of this domain consists of two layers, alpha/beta, which contain an 8-stranded mixed beta-sheet.[2]
Subfamilies
- Heat shock protein Hsp90, N-terminal
- Sensor histidine kinase NatK, C-terminal domain
Members
- BCKDK
- HSP90AA1, HSP90AB1, HSP90B1
- MLH1, MLH3, MORC1, MORC2, MORC3, MORC4
- PDK1, PDK2, PDK3, PDK4
- PMS1, PMS2, PMS2L1, PMS2L11, PMS2L3, PMS4L
- TOP2A, TOP2B
- TRAP1, TRRAP
References
- ↑ "A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone". Nat. Struct. Biol. 4 (6): 477–82. June 1997. doi:10.1038/nsb0697-477. PMID 9187656.
- ↑ Jump up to: 2.0 2.1 "GHKL, an emergent ATPase/kinase superfamily". Trends Biochem. Sci. 25 (1): 24–8. January 2000. doi:10.1016/S0968-0004(99)01503-0. PMID 10637609.
- ↑ "Crystal Structures of Escherichia coli Topoisomerase IV ParE Subunit (24 and 43 Kilodaltons): a Single Residue Dictates Differences in Novobiocin Potency against Topoisomerase IV and DNA Gyrase". Antimicrob. Agents Chemother. 48 (5): 1856–64. May 2004. doi:10.1128/AAC.48.5.1856-1864.2004. PMID 15105144.
- ↑ "Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone". J. Biol. Chem. 279 (44): 46162–71. October 2004. doi:10.1074/jbc.M405253200. PMID 15292259.
- ↑ "The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)". Cell 116 (1): 87–98. January 2004. doi:10.1016/S0092-8674(03)01027-4. PMID 14718169.
- ↑ "Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms". Chem. Biol. 11 (6): 775–85. June 2004. doi:10.1016/j.chembiol.2004.03.033. PMID 15217611.
- ↑ McDowall J (2006). "DNA Topoisomerase". Protein of the month. InterPro. http://www.ebi.ac.uk/interpro/potm/2006_1/Page1.htm.
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